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Two heat-stable and trypsin-labile inhibitors of phosphorylase phosphatase, designated inhibitor-1 and inhibitor-2, were partially purified from extracts of rabbit skeletal muscle by heating and coloumn chromatography using DEAE-dellulose and Bio-gel P-60. Inhibitor-1 exists in an active phosphorylated form and an inactive dephosphorylated form. The interconversion of phosphorylated inhibitor-1 and dephosphorylated inhibitor-1 is mediated by protein kinase dependent on adenosine 3':5'-monophosphate (cyclic AMP) and a Mn2+-stimulated phosphoprotein phosphatase. Inhibitory activity of inhibitor-2 is not influenced by treatment with either the kinase or the Mn2+-stimulated phosphatase. The molecular weights of inhibitor-1 and inhibitor-2 estimated by sodium dodecylsulfate-polyacrylamide gel electrophoresis are 26000 and 33000 respectively. Both inhibitor-1 and inhibitor-2 inhibit phosphorylase phosphatase by a mechanism which appears to be non-competitive with respect to the substrate phosphorylase a. Inhibitor fractions at early stages of purification also inhibit cyclic-AMP-dependent histone phosphorylation, but this kinase inhibitory activity resides with a protein moiety which is separable from inhibitor-1 and inhibitor-2.
F L Huang, and
W H Glinsmann
January 1975,
Biochemical Society transactions,
F L Huang, and
W H Glinsmann
January 1988,
Methods in enzymology,
F L Huang, and
W H Glinsmann
September 1976,
European journal of biochemistry,
F L Huang, and
W H Glinsmann
December 1983,
Biochemical and biophysical research communications,
F L Huang, and
W H Glinsmann
April 1977,
Molecular and cellular biochemistry,
F L Huang, and
W H Glinsmann
December 1987,
European journal of biochemistry,
F L Huang, and
W H Glinsmann
January 1983,
Methods in enzymology,
F L Huang, and
W H Glinsmann
November 1974,
Biochimica et biophysica acta,
F L Huang, and
W H Glinsmann
September 1987,
Biochimica et biophysica acta,
F L Huang, and
W H Glinsmann
April 1977,
Molecular and cellular biochemistry,
